AC MF_00419; DC Protein; auto TR HAMAP; MF_00419; -; 1; level=0 XX Names: PurL_1 XX ID PUR4 DE RecName: Full=Phosphoribosylformylglycinamidine synthase; DE Short=FGAM synthase; DE Short=FGAMS; DE EC=6.3.5.3; DE AltName: Full=Formylglycinamide ribonucleotide amidotransferase; DE Short=FGAR amidotransferase; DE Short=FGAR-AT; GN Name=purL; XX CC -!- FUNCTION: Phosphoribosylformylglycinamidine synthase involved in the CC purines biosynthetic pathway. Catalyzes the ATP-dependent conversion of CC formylglycinamide ribonucleotide (FGAR) and glutamine to yield CC formylglycinamidine ribonucleotide (FGAM) and glutamate. CC -!- CATALYTIC ACTIVITY: CC Reaction=ATP + H2O + L-glutamine + N(2)-formyl-N(1)-(5-phospho-beta-D- CC ribosyl)glycinamide = 2-formamido-N(1)-(5-O-phospho-beta-D- CC ribosyl)acetamidine + ADP + H(+) + L-glutamate + phosphate; CC Xref=Rhea:RHEA:17129, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:29985, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, CC ChEBI:CHEBI:58359, ChEBI:CHEBI:147286, ChEBI:CHEBI:147287, CC ChEBI:CHEBI:456216; EC=6.3.5.3; CC -!- PATHWAY: Purine metabolism; IMP biosynthesis via de novo pathway; 5- CC amino-1-(5-phospho-D-ribosyl)imidazole from N(2)-formyl-N(1)-(5- CC phospho-D-ribosyl)glycinamide: step 1/2. CC -!- SUBUNIT: Monomer. CC -!- SUBCELLULAR LOCATION: Cytoplasm. CC -!- SIMILARITY: In the N-terminal section; belongs to the FGAMS family. XX DR Pfam; PF00586; AIRS; 1; trigger=no DR PROSITE; PS51273; GATASE_TYPE_1; 1; trigger=yes DR NCBIfam; TIGR01735; FGAM_synt; 1; trigger=no XX KW ATP-binding KW Cytoplasm KW Glutamine amidotransferase KW Ligase KW Metal-binding KW Magnesium KW Nucleotide-binding KW Purine biosynthesis XX GO GO:0005524; F:ATP binding GO GO:0004642; F:phosphoribosylformylglycinamidine synthase activity GO GO:0006189; P:'de novo' IMP biosynthetic process GO GO:0005737; C:cytoplasm XX FT From: PUR4_SALTY (P74881) FT BINDING 307..318 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT Optional; Condition: G-A-[SA]-T-G-[SAVI]-G-G-E-I-R-D FT BINDING 386..388 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT Optional; Condition: T-G-Y FT ACT_SITE 1135 FT /note="Nucleophile" FT Condition: C FT ACT_SITE 1260 FT Condition: H FT ACT_SITE 1262 FT Condition: E FT BINDING 679 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT Condition: D FT BINDING 718 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT Condition: E FT BINDING 722 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT Condition: N FT BINDING 884 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT Condition: D FT BINDING 678 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT Condition: A FT BINDING 886 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT Condition: S XX Size: 1293-1369; Related: MF_00420; MF_00421; Template: P15254; P74881; Scope: Bacteria Fusion: Nter: None Cter: None Duplicate: None Plasmid: None Comments: FGAM synthase can be composed of a single polypeptide (large PurL, MF_00419), or it can be composed of three separate proteins: PurL (small PurL, MF_00420), PurQ (MF_00421) and PurS (MF_01926). XX # Revision 1.47 2023/06/01 //